GenomeNet

Database: UniProt
Entry: A0A2J9E1W9_9GAMM
LinkDB: A0A2J9E1W9_9GAMM
Original site: A0A2J9E1W9_9GAMM 
ID   A0A2J9E1W9_9GAMM        Unreviewed;       468 AA.
AC   A0A2J9E1W9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE            Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN   Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563};
GN   ORFNames=A6J60_012925 {ECO:0000313|EMBL:PNK61679.1};
OS   Psychrobacter sp. FDAARGOS_221.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK61679.1, ECO:0000313|Proteomes:UP000217719};
RN   [1] {ECO:0000313|Proteomes:UP000217719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA   Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA   Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA   Aluvathingal J., Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a key role in the regulation of the intracellular
CC       concentration of adenosylhomocysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_00563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|RuleBase:RU000548};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC         ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|PIRSR:PIRSR001109-2, ECO:0000256|RuleBase:RU000548};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC       ECO:0000256|RuleBase:RU004166}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNK61679.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NWFK02000001; PNK61679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J9E1W9; -.
DR   OrthoDB; 9802717at2; -.
DR   UniPathway; UPA00314; UER00076.
DR   Proteomes; UP000217719; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   NCBIfam; TIGR00936; ahcY; 1.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000256|RuleBase:RU000548};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00563}.
FT   DOMAIN          204..380
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         170..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-1"
FT   BINDING         204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         233..238
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         235..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         305
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT   BINDING         326..328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         374
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT                   ECO:0000256|PIRSR:PIRSR001109-2"
FT   BINDING         381
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ   SEQUENCE   468 AA;  51609 MW;  BE5824E88A9A0649 CRC64;
     MDAVSNIDSS FTDYKVADIS LADYGRREIS LAEAEMPALM GLRKRYSEQQ PLAGAKILGC
     IHMTIQTAVL IETLVALGAE VRWTSCNIFS TQDHAAAAMA ANGIPVFAWK GETEEEYEWC
     LRQQLFVGGE ENGELWDANL ILDDGGDLTA LIHNDYPQML DTINGISEET TTGVHRLIEM
     LNKGTLKVPA INVNDAVTKS KNDNKYGCRH SLNDAIKRGT DMLLAGRRAL VIGYGDVGKG
     SAQSLRQEGM IVRVTEVDPI CAMQACMDGY ELVSPYIDGN NTNSAEGINT RLLQDTDLIV
     TTTGNYHVCD KHMLAALKSG AVVCNIGHFD TEIDTQFMRD NWRWEEIKPQ VHQVYRSEED
     GDYLILLAEG RLVNLGNATG HPSRVMDGSF ANQVLAQMYL HEQNFSELPA DERANGLYVK
     VLPKKLDEEV AAAMVAGFNG VMTKLTPEQA DYIGVPVEGP FKPNDYKY
//
DBGET integrated database retrieval system